1ie0

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{{Seed}}
 
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[[Image:1ie0.png|left|200px]]
 
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==CRYSTAL STRUCTURE OF LUXS==
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The line below this paragraph, containing "STRUCTURE_1ie0", creates the "Structure Box" on the page.
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<StructureSection load='1ie0' size='340' side='right'caption='[[1ie0]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ie0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IE0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IE0 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1ie0| PDB=1ie0 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ie0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ie0 OCA], [https://pdbe.org/1ie0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ie0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ie0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ie0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LUXS_BACSU LUXS_BACSU] Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).[HAMAP-Rule:MF_00091]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ie/1ie0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ie0 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The ability of bacteria to regulate gene expression in response to changes in cell density is termed quorum sensing. This behavior involves the synthesis and recognition of extracellular, hormone-like compounds known as autoinducers. Here we report the structure of an autoinducer synthase, LuxS from Bacillus subtilis, at 1.6-A resolution (R(free) = 0.204; R(work) = 0.174). LuxS is a homodimeric enzyme with a novel fold that incorporates two identical tetrahedral metal-binding sites. This metal center is composed of a Zn(2+) atom coordinated by two histidines, a cysteine, and a solvent molecule, and is reminiscent of active sites found in several peptidases and amidases. Although the nature of the autoinducer synthesized by LuxS cannot be deduced from the crystal structure, features of the putative active site suggest that LuxS might catalyze hydrolytic, but not proteolytic, cleavage of a small substrate. Our analysis represents a test of structure-based functional assignment.
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===CRYSTAL STRUCTURE OF LUXS===
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Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site.,Hilgers MT, Ludwig ML Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11169-74. Epub 2001 Sep 11. PMID:11553770<ref>PMID:11553770</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_11553770}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1ie0" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11553770 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11553770}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1IE0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IE0 OCA].
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==Reference==
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Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site., Hilgers MT, Ludwig ML, Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11169-74. Epub 2001 Sep 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11553770 11553770]
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hilgers, M T.]]
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[[Category: Hilgers MT]]
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[[Category: Ludwig, M L.]]
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[[Category: Ludwig ML]]
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[[Category: Cysteine-sulfonic acid]]
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[[Category: Four stranded antiparallel beta sheet]]
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[[Category: Structural genomic]]
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[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:49:28 2008''
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Current revision

CRYSTAL STRUCTURE OF LUXS

PDB ID 1ie0

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